Article
An approach to optimizing the active site in a glutathione transferase by evolution in vitro.
The Biochemical journal - 15 Nov 1999
Hansson L O, Widersten M, Mannervik B
Abstract excerpt
A glutathione transferase (GST) mutant with four active-site substitutions (Phe(10)-->Pro/Ala(12)-->Trp/Leu(107)-->Phe/Leu(108)-->Arg) (C36) was isolated from a library of active-site mutants of human GST A1-1 by the combination of phage display and mechanism-based affinity adsorption [Hansson, Widersten and Mannervik (1997) Biochemistry 36, 11252-11260]. C36 was selected on the basis of its affinity for the...
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